ID U1NQ27_9EURY Unreviewed; 392 AA.
AC U1NQ27;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_01244};
DE Short=DHQ synthase {ECO:0000256|HAMAP-Rule:MF_01244};
DE EC=1.4.1.24 {ECO:0000256|HAMAP-Rule:MF_01244};
DE AltName: Full=3-dehydroquinate synthase II {ECO:0000256|HAMAP-Rule:MF_01244};
GN Name=aroB' {ECO:0000256|HAMAP-Rule:MF_01244};
GN ORFNames=J07HQX50_00752 {ECO:0000313|EMBL:ERG99605.1};
OS Haloquadratum sp. J07HQX50.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=1238426 {ECO:0000313|EMBL:ERG99605.1, ECO:0000313|Proteomes:UP000030642};
RN [1] {ECO:0000313|EMBL:ERG99605.1, ECO:0000313|Proteomes:UP000030642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HQX50 {ECO:0000313|Proteomes:UP000030642};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
CC -!- FUNCTION: Catalyzes the oxidative deamination and cyclization of 2-
CC amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-
CC dehydroquinate (DHQ), which is fed into the canonical shikimic pathway
CC of aromatic amino acid biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01244}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)
CC = 3-dehydroquinate + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:25956,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58859; EC=1.4.1.24; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01244};
CC -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_01244}.
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DR EMBL; KE356562; ERG99605.1; -; Genomic_DNA.
DR AlphaFoldDB; U1NQ27; -.
DR STRING; 1238426.J07HQX50_00752; -.
DR HOGENOM; CLU_056379_0_0_2; -.
DR Proteomes; UP000030642; Unassembled WGS sequence.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR GO; GO:0102042; F:dehydroquinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01244; Arch_DHQ_synthase; 1.
DR InterPro; IPR002812; DHQ_synth.
DR PANTHER; PTHR33563; -; 1.
DR PANTHER; PTHR33563:SF1; 3-DEHYDROQUINATE SYNTHASE; 1.
DR Pfam; PF01959; DHQS; 1.
DR PIRSF; PIRSF006655; DHQ_synth; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01244};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_01244}; NAD {ECO:0000256|HAMAP-Rule:MF_01244};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01244}; Reference proteome {ECO:0000313|Proteomes:UP000030642}.
SQ SEQUENCE 392 AA; 42945 MW; F8D0CF50BD8F50FD CRC64;
MTRSVWLKAD NSVGEWETRK QRITTGLEAG VDWVLVDEAD ITRVRRLGDV NVAAFYSDTE
TSIIDNAEVD SMDAQTPEAY IIGKDSEGDA TIDLPDELSS SADLTALRRN EEAASGAYIR
ILSEQYETFA QTAAEEAHYT IVIGEDWTII PLENLIARIG DETGLIAGVT SADEAKTAFE
TLELGADGVL LDSGDADEIH QTVKVRDEAD REVIDLEWAT VTGVERTGMA DRVCVDTGTL
LEHNEGMLVG SMSRGLFFVH AETADSPYVA SRPFRVNAGA VHAYIRTPDG GTKYLSELKS
GDTVQVVNAE GKTREVVVGR VKIEKRPMFR VETEVGGDRI ETLLQNAETI KVHTKNGHTA
VTDLEPGDEM ALFHQEGARH FGERIEESII EK
//
